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- W2026520199 abstract "Serotonin and benzylamine oxidising activities of membrane-bound rat liver monoamine oxidase have been distinguished according to their sensitivities towards 5-phenyl-3-(N-cyclopropyl)ethylamine-1, 2,4-oxadiazole (PCO). Tyramine, tryptamine and dopamine deamination have been shown to exhibit dual sensitivities to PCO inhibition, corresponding to these monoamines undergoing oxidation at both the PCO sensitive and insensitive sites responsible for serotonin and benzylamine oxidation respectively. The biphasic inhibition of tyramine deamination by PCO is shown to result from ‘fast’ and ‘slow’ pseudo-first order reactions with the enzyme. Both ‘fast’ and ‘slow’' reactions are shown to have two components, of which the slower is quantitatively the most important. The corresponding 3-nitrophenyl compound (3-nitro-PCO) preferentially inhibits tyramine oxidation at low concentrations. This is shown to result from a reversal of the relative rates of attack, by this inhibitor, on the two centres of deamination. PCO has been shown to be a potent instantaneous competitive inhibitor of the enzyme. With serotonin as substrate a Ki of 10−7M was obtained. An enzyme with serotonin oxidation completely blocked by PCO or 2-chloro-PCO, but retaining approximately half the tyramine deaminating activity has been prepared. The kinetic parameters for the oxidation of tyramine, tryptamine and dopamine by such partially inhibited preparations have been determined." @default.
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- W2026520199 title "Studies on the selective inhibition of membrane-bound rat liver monoamine oxidase" @default.
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- W2026520199 doi "https://doi.org/10.1016/0006-2952(75)90099-4" @default.
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